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METL_AQUAE
ID   METL_AQUAE              Reviewed;         400 AA.
AC   O67275;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable S-adenosylmethionine synthase;
DE            Short=AdoMet synthase;
DE            EC=2.5.1.6;
DE   AltName: Full=Methionine adenosyltransferase;
GN   Name=mat; OrderedLocusNames=aq_1226;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-
CC         adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase 2 family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07239.1; -; Genomic_DNA.
DR   PIR; H70405; H70405.
DR   RefSeq; NP_213839.1; NC_000918.1.
DR   RefSeq; WP_010880777.1; NC_000918.1.
DR   AlphaFoldDB; O67275; -.
DR   SMR; O67275; -.
DR   STRING; 224324.aq_1226; -.
DR   EnsemblBacteria; AAC07239; AAC07239; aq_1226.
DR   KEGG; aae:aq_1226; -.
DR   PATRIC; fig|224324.8.peg.954; -.
DR   eggNOG; COG1812; Bacteria.
DR   HOGENOM; CLU_057642_0_0_0; -.
DR   InParanoid; O67275; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 468241at2; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.300.280; -; 1.
DR   HAMAP; MF_00136; S_AdoMet_synth2; 1.
DR   InterPro; IPR027790; AdoMet_synthase_2_family.
DR   InterPro; IPR042544; AdoMet_synthase_3.
DR   InterPro; IPR002795; S-AdoMet_synthetase_arc.
DR   PANTHER; PTHR36697; PTHR36697; 1.
DR   Pfam; PF01941; AdoMet_Synthase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; One-carbon metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..400
FT                   /note="Probable S-adenosylmethionine synthase"
FT                   /id="PRO_0000150045"
FT   BINDING         135..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  45040 MW;  516E81FA05E856E9 CRC64;
     MKNIVVTPMT FEPVYEQDAE IVERKGIGHP DTICDYLAEE LSVALSKLYI ERFGAIMHHN
     VDKALLVGGE ANPVFGGGEV ISPIEIYLVG RALKEYKGVT IPAEELAIEV AREWLKDNIR
     NLDPDTHVII KPRIKPGSKD LVDLFLRFQQ KGEVPLANDT SFGVGFAPLD DLERIVFETE
     QLLNSPSFKE NHPYVGEDIK VMGVRIKDKV RITIACAFVS KYVENIQDYL EKKEHVRRIV
     EEMAQGLTQR QVEVFINTAD DPERESVYIT VTGTSAEQGD DGQVGRGNRV NGLITPYRPM
     SLEAAAGKNP VSHIGKIYNV VANVIADRVV SEIEEVEEAY CYLVSQIGKP INEPQVCDVK
     VRTKKDLKSL EEEIKRIAQE ELEKMPETWK KFLNREYAVA
 
 
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